We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Apomyoglobin stability as dependent on urea concentration and temperature at two pH values.
- Authors
Baryshnikova, E. N.; Sharapov, M. G.; Kashparov, I. A.; Ilyina, N. B.; Bychkova, V. E.
- Abstract
Equilibrium unfolding of apomyoglobin (ApoMb) in the presence of urea was studied as dependent on the temperature (5-2°C) at two pH values (5.7 and 6.2). Thermodynamic parameters of ApoMb transition from the native to the unfolded state were estimated under various conditions. Conformational changes in ApoMb were detected by tryptophan fluorescence and far-UV circular dichroism. The ApoMb stability and the cooperativity of its unfolding at 5°C were considerably lower than at other temperatures at both pH values, where ApoMb is in the native conformation.
- Subjects
THERMODYNAMICS; UREA; TRYPTOPHAN; AMINO acids; DICHROISM; METABOLISM
- Publication
Molecular Biology, 2005, Vol 39, Issue 2, p292
- ISSN
0026-8933
- Publication type
Article
- DOI
10.1007/s11008-005-0041-9